Resolve Complex Structures
Advanced Structural Biology and Native MS
Build native MS, surface-induced dissociation, and charge-reduction workflows that reveal protein-complex interfaces, topology, and heterogeneous assemblies.
How Researchers Use Our Products
How Researchers Use Ardara
Explore the instrument challenge, the Ardara solution selected, and the performance reported by each research team.
Used by researchers
2019
The Ohio State University
Relative Interfacial Cleavage Energetics of Protein Complexes Revealed by Surface Collisions
- Solution used
- External multichannel power supply controlling ten surface-induced dissociation lenses
An external Ardara supply controlled ten DC lenses in a surface-induced dissociation device used to interrogate protein-complex interfaces. By varying collision conditions, the team showed that low-energy surface collisions preferentially cleave the weakest interfaces and developed a predictive model using structural interface features. The Ardara supply enabled coordinated control of the SID ion optics, supporting a workflow that linked gas-phase fragmentation patterns to native protein topology and assembly.
Published by Harvey et al. in Proceedings of the National Academy of Sciences (2019).
Used by researchers
2024
The Ohio State University
Protein Complex Heterogeneity and Topology Revealed by Electron Capture Charge Reduction and Surface Induced Dissociation
- Solution used
- External DC supplies for C-trap offset and surface-induced dissociation voltages
Ardara external supplies provided the C-trap DC offset and surface-induced dissociation voltages in a platform combining electron capture charge reduction with SID. The system was applied to GroEL, a SARS-CoV-2 spike construct, thyroglobulin, and the 50S ribosomal subunit, including charge-reduced signals beyond m/z 100,000. The work shows Ardara voltage control supporting analysis of exceptionally large and heterogeneous assemblies while preserving topology-relevant fragmentation information.
Published by Shaw et al. in ACS Central Science (2024).
Co-developed with Ardara
2017
The Ohio State University, Pacific Northwest National Laboratory, Bruker, and Ardara Technologies
Surface-Induced Dissociation of Protein Complexes in a Hybrid Fourier Transform Ion Cyclotron Resonance Mass Spectrometer
- Solution used
- Custom surface-induced dissociation device integrated into a 15 T Bruker SolariX XR
The team installed a custom SID assembly in place of the collision cell in a 15 T FT-ICR instrument. With Ardara's Randall Pedder as a coauthor, the collaboration demonstrated surface-collision analysis of protein complexes from 53 to 85 kDa and obtained isotopically resolved fragment and ligand signals. The paper documents Ardara participation in both the instrumentation and the scientific validation of a new structural-biology workflow, making it stronger evidence than a product mention alone.
Published by Yan et al.; Randall E. Pedder was an Ardara-affiliated coauthor in Analytical Chemistry (2017).
Plan Your Instrument with Ardara
Share your pressure regime, target mass range, RF or DC requirements, geometry, and control constraints. Our team can help match catalog components to your design or define a custom subsystem.